ID A0A418NWI3_9SPHN Unreviewed; 664 AA.
AC A0A418NWI3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:RIV88999.1};
GN ORFNames=D2V07_01670 {ECO:0000313|EMBL:RIV88999.1};
OS Aurantiacibacter zhengii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=2307003 {ECO:0000313|EMBL:RIV88999.1, ECO:0000313|Proteomes:UP000286576};
RN [1] {ECO:0000313|EMBL:RIV88999.1, ECO:0000313|Proteomes:UP000286576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V18 {ECO:0000313|EMBL:RIV88999.1,
RC ECO:0000313|Proteomes:UP000286576};
RA Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA Xu X.-W.;
RT "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT sediment.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RIV88999.1}.
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DR EMBL; QXFL01000001; RIV88999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418NWI3; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000286576; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286576};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RIV88999.1}.
FT DOMAIN 350..521
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 664 AA; 71601 MW; B4347934C959A6B5 CRC64;
MSDDTARFTN MANAIRALSM DAVQAANSGH PGMPMGMADV AAVLWSDYLK FDPKAPDWAD
RDRFVLSAGH GSMLIYSLLH LSGYDQPTLE DIRNFRQLGS PCAGHPENFL LPGVEATTGP
LGQGVAMAVG MAMAERHLNA QFGDDLVDHR TWAIAGDGCL MEGINHEAIG IAGHLRLGRL
TVLWDDNDIT IDGKVSLSSS EDIPARYRAT GWHVVKCDGH DPADIRRALD EAVAETDRPS
LVQCTTIIGK GAPNKQGTSA THGAPLGEDE IAAARKELGW DHGPFEVPED IRADWLATAK
RGTAAHAEWQ DRLSGSKDKA EFTRRMSGEL PAGDKAARAF SKWLESAEKV ATRKASENAL
DVLNPLVPEL VGGSADLTGS NNTKAGGIGP FTADDYSGRY VYYGIREFGM SAAMNGMALH
GGIIPYGGTF LIFTDYCRGA IRLSALQECR VVYVMTHDSI GLGEDGPTHQ PIEHLQSLRA
MPNLLVMRPA DRVETAECWQ IAIAQKNRPS VIALSRQGLP QVRNSPEETD MCSKGGYRLK
RAGNKRRVIL IATGSEVSLA LECADQLEKQ GVGADVVSMV CTELFDEQDA AYKEDILPNV
GPDQILRVSI EAGTTFGWER YTMANGLNIG IDRFGASAPA GDLFKKFGLT ADAIVPKIIS
KLND
//
